MTMR9_BOVIN
ID MTMR9_BOVIN Reviewed; 549 AA.
AC A7MB43;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Myotubularin-related protein 9 {ECO:0000305};
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 9 {ECO:0000305};
GN Name=MTMR9 {ECO:0000312|VGNC:VGNC:50009};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|EMBL:AAI51330.1};
RN [1] {ECO:0000312|EMBL:AAI51330.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI51330.1};
RC TISSUE=Fetal brain {ECO:0000312|EMBL:AAI51330.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136};
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Acts as an adapter for myotubularin-related phosphatases.
CC Increases lipid phosphatase MTMR6 catalytic activity, specifically
CC towards phosphatidylinositol 3,5-bisphosphate, and MTMR6 binding
CC affinity for phosphorylated phosphatidylinositols (By similarity).
CC Positively regulates lipid phosphatase MTMR7 catalytic activity (By
CC similarity). Increases MTMR8 catalytic activity towards
CC phosphatidylinositol 3-phosphate. The formation of the MTMR6-MTMR9
CC complex, stabilizes both MTMR6 and MTMR9 protein levels. Stabilizes
CC MTMR8 protein levels. Plays a role in the late stages of
CC macropinocytosis possibly by regulating MTMR6-mediated
CC dephosphorylation of phosphatidylinositol 3-phosphate in membrane
CC ruffles. Negatively regulates autophagy, in part via its association
CC with MTMR8. Negatively regulates DNA damage-induced apoptosis, in part
CC via its association with MTMR6. Does not bind mono-, di- and tri-
CC phosphorylated phosphatidylinositols, phosphatidic acid and
CC phosphatidylserine (By similarity). {ECO:0000250|UniProtKB:Q96QG7,
CC ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- SUBUNIT: Homodimer. Heterodimer (via C-terminus) with lipid phosphatase
CC MTMR6 (via C-terminus) (By similarity). Heterodimer (via coiled coil
CC domain) with lipid phosphatase MTMR7 (via C-terminus) (By similarity).
CC Heterodimer with lipid phosphatase MTMR8 (By similarity).
CC {ECO:0000250|UniProtKB:Q96QG7, ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96QG7}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q96QG7}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96QG7}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q96QG7}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q96QG7}. Note=Localizes to ruffles during EGF-
CC induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the
CC perinuclear region. Partially localizes to the endoplasmic reticulum
CC (By similarity). {ECO:0000250|UniProtKB:Q96QG7,
CC ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- DOMAIN: The GRAM domain is required for cell membrane localization.
CC {ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- DOMAIN: The coiled coil domain mediates interaction with MTMR9.
CC {ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000255}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 333 in the dsPTPase catalytic loop, suggesting that it has no
CC phosphatase activity. {ECO:0000305}.
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DR EMBL; BC151329; AAI51330.1; -; mRNA.
DR EMBL; DAAA02021925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001094657.1; NM_001101187.2.
DR AlphaFoldDB; A7MB43; -.
DR SMR; A7MB43; -.
DR STRING; 9913.ENSBTAP00000004852; -.
DR PaxDb; A7MB43; -.
DR PRIDE; A7MB43; -.
DR Ensembl; ENSBTAT00000004852; ENSBTAP00000004852; ENSBTAG00000003726.
DR GeneID; 539174; -.
DR KEGG; bta:539174; -.
DR VEuPathDB; HostDB:ENSBTAG00000003726; -.
DR VGNC; VGNC:50009; MTMR9.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000157818; -.
DR HOGENOM; CLU_001839_3_1_1; -.
DR OMA; RHENGAT; -.
DR OrthoDB; 824298at2759; -.
DR TreeFam; TF315197; -.
DR Reactome; R-BTA-1660499; Synthesis of PIPs at the plasma membrane.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000003726; Expressed in semen and 108 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IEA:Ensembl.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..549
FT /note="Myotubularin-related protein 9"
FT /id="PRO_0000446365"
FT DOMAIN 4..99
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 123..498
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT COILED 508..542
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96QG7"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QG7"
SQ SEQUENCE 549 AA; 63486 MW; DEA093883957B00F CRC64;
MEFAELIKTP RVDNVVLHRP FYPAVEGTLC LTGHHLILSS RQDNTEELWL LHSNIDAIDK
RFVGPLGTII IKCKDFRIIQ LDIPGMEECL NIASSIEALS TLDSITLMYP FFYRPMFEVI
EDGWHSFLPE QEFELYSSTI SEWRLSYVNK EFSVCPSYPP AVIVPKAIDD DALRKVATFR
HGGRFPVLSY YHKKNGMVIM RSGQPLTGTN GRRCKEDEKL INATLRAGKR GYIIDTRPLN
IAQQARAKGG GFEQEAHYPQ WRRIHKSIDR YHILQESLIK LVESCNDQTQ NMDRWLSKLE
ASNWLTHIKE ILTTACLAAQ CLDREGASIL IHGTEGTDST LQVTSLAQII LEPRSRTIRG
FEALIEREWL QAGHPFQQRC AQSAYCNSKQ KWESPVFLLF LDCVWQILRQ FPCSFEFNEN
FLIMLFEHAY ASQFGTFLGN NESERCKLKL QQKTMSLWSW VNRPSELSKF TNPLFEANNL
VIWPSVAPQS LQLWEGIFLR WNRSSKYLDE AYEEMVNIIE YNKELQAKVN LLRRQLAELE
TEDGVQESP
